STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
KPU44581.1Stage II sporulation protein R (spore_II_R). (239 aa)    
Predicted Functional Partners:
gerBA_2
Spore germination protein B1.
 
    0.867
spoIIGA
Sporulation sigma-E factor-processing peptidase; Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR. Belongs to the peptidase U4 family.
 
   
 0.864
spoIIID
Stage III sporulation protein D.
  
   
 0.857
KPU44923.1
Hypothetical protein.
  
  
 0.852
spoIIE
Stage II sporulation protein E.
  
   
 0.852
spoIVA
Stage IV sporulation protein A; ATPase. Has a role at an early stage in the morphogenesis of the spore coat.
  
   
 0.846
spoVT
Stage V sporulation protein T.
  
   
 0.843
KPU44130.1
Stage II sporulation protein P (SpoIIP).
  
   
 0.842
KPU44113.1
Putative stage IV sporulation protein YqfD.
  
  
 0.840
spoIIAB
Anti-sigma F factor; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
  
   
 0.839
Your Current Organism:
Oxobacter pfennigii
NCBI taxonomy Id: 36849
Other names: ATCC 43583, Clostridium pfennigii, DSM 3222, O. pfennigii, strain V5-2
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